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Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors

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Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors. / Nett, Isabelle R. E.; Mehlert, Angela; Lamont, Douglas; Ferguson, Michael A. J.

In: Glycobiology, Vol. 20, No. 5, 05.2010, p. 576-585.

Research output: Contribution to journalArticle

Harvard

Nett, IRE, Mehlert, A, Lamont, D & Ferguson, MAJ 2010, 'Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors' Glycobiology, vol 20, no. 5, pp. 576-585.

APA

Nett, I. R. E., Mehlert, A., Lamont, D., & Ferguson, M. A. J. (2010). Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors. Glycobiology, 20(5), 576-585doi: 10.1093/glycob/cwq007

Vancouver

Nett IRE, Mehlert A, Lamont D, Ferguson MAJ. Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors. Glycobiology. 2010 May;20(5):576-585.

Author

Nett, Isabelle R. E.; Mehlert, Angela; Lamont, Douglas; Ferguson, Michael A. J. / Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors.

In: Glycobiology, Vol. 20, No. 5, 05.2010, p. 576-585.

Research output: Contribution to journalArticle

Bibtex - Download

@article{aac46229dc7f4a7fb4455986eb1b3470,
title = "Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors",
author = "Nett, {Isabelle R. E.} and Angela Mehlert and Douglas Lamont and Ferguson, {Michael A. J.}",
year = "2010",
volume = "20",
number = "5",
pages = "576--585",
journal = "Glycobiology",
issn = "0959-6658",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors

A1 - Nett,Isabelle R. E.

A1 - Mehlert,Angela

A1 - Lamont,Douglas

A1 - Ferguson,Michael A. J.

AU - Nett,Isabelle R. E.

AU - Mehlert,Angela

AU - Lamont,Douglas

AU - Ferguson,Michael A. J.

PY - 2010/5

Y1 - 2010/5

N2 - <p>The addition of glycosylphosphatidylinositol (GPI) anchors to proteins is an important posttranslational modification in eukaryotic cells. The complete structural elucidation of GPI anchors is a complex process that requires relatively large amounts of starting material. In this paper, we assess the degree of structural information that can be obtained by applying electrospray mass spectrometry and tandem mass spectrometry to permethylated GPI glycans prepared from a well-characterized GPI-anchored glycoprotein, the variant surface glycoprotein from Trypanosoma brucei. All GPI glycans contain a non-N-acetylated glucosamine residue, and permethylation leads to the formation of a fixed positive charge on the glycans, in the form of a quaternary amine. The permethylated glycans were detected as [M +- Na](2+-) ions, and tandem mass spectrometry of these ions produced substantial, albeit incomplete, structural information on the branching patterns and linkage types for various GPI glycoforms of the variant surface glycoprotein.</p>

AB - <p>The addition of glycosylphosphatidylinositol (GPI) anchors to proteins is an important posttranslational modification in eukaryotic cells. The complete structural elucidation of GPI anchors is a complex process that requires relatively large amounts of starting material. In this paper, we assess the degree of structural information that can be obtained by applying electrospray mass spectrometry and tandem mass spectrometry to permethylated GPI glycans prepared from a well-characterized GPI-anchored glycoprotein, the variant surface glycoprotein from Trypanosoma brucei. All GPI glycans contain a non-N-acetylated glucosamine residue, and permethylation leads to the formation of a fixed positive charge on the glycans, in the form of a quaternary amine. The permethylated glycans were detected as [M +- Na](2+-) ions, and tandem mass spectrometry of these ions produced substantial, albeit incomplete, structural information on the branching patterns and linkage types for various GPI glycoforms of the variant surface glycoprotein.</p>

KW - glycosylphosphatidylinositol

KW - GPI anchor

KW - mass spectrometry

KW - Trypanosoma brucei

KW - variant surface glycoprotein

KW - VARIANT SURFACE GLYCOPROTEIN

KW - TRYPANOSOMA-BRUCEI

KW - PROTEIN

KW - MS

U2 - 10.1093/glycob/cwq007

DO - 10.1093/glycob/cwq007

M1 - Article

JO - Glycobiology

JF - Glycobiology

SN - 0959-6658

IS - 5

VL - 20

SP - 576

EP - 585

ER -

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